Pressure stability of the α‐helix structure in a de novo designed protein (α‐l‐α)2 studied by FTIR spectroscopy

The pressure‐induced structural changes of a de novo designed four‐helix bundle protein, (α‐l‐α)2, in aqueous solution have been investigated by FTIR spectroscopy. Changes in the amide I' band intensity show that pressure induces disruption of tertiary interactions and stabilizes the solvated α‐helical form. This may suggest that the exposure of the hydrophobic core to the solvent by pressure is not a sufficient condition for pressure‐induced unfolding of the α‐helices of proteins. © 2006 Wiley Periodicals, Inc. Biopolymers 85:185–188, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com